Molecular and biochemical characterization of a novel xylanase from the symbiotic Sphingobacterium sp. TN19

@article{Zhou2009MolecularAB,
  title={Molecular and biochemical characterization of a novel xylanase from the symbiotic Sphingobacterium sp. TN19},
  author={Junpei Zhou and Huo-qing Huang and Kun Meng and Pengjun Shi and Yaru Wang and Huiying Luo and Peilong Yang and Yingguo Bai and Zhigang Zhou and Bin Yao},
  journal={Applied Microbiology and Biotechnology},
  year={2009},
  volume={85},
  pages={323-333}
}
A xylanase-encoding gene, designated xynA19, was cloned from Sphingobacterium sp. TN19—a symbiotic bacterium isolated from the gut of Batocera horsfieldi larvae—and expressed in Escherichia coli BL21 (DE3). The full-length xynA19 (1,155 bp in length) encodes a 384-residue polypeptide (XynA19) containing a predicted signal peptide of 24 residues and a catalytic domain belonging to glycosyl hydrolase family 10 (GH 10). The deduced amino acid sequence of XynA19 is most similar (53.1% identity) to… CONTINUE READING

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